STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
leuB3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily. (336 aa)    
Predicted Functional Partners:
leuC
3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
 0.998
leuD
3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
 
 
 0.997
Mvan_2123
TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT domain protein; KEGG: mmc:Mmcs_1907 acetolactate synthase, small subunit.
 
 0.995
Mvan_2122
TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: mmc:Mmcs_1906 acetolactate synthase, large subunit, biosynthetic type.
 
 0.985
Mvan_1352
PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: mpa:MAP4208 hypothetical protein.
 
 0.974
Mvan_4954
PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme, central region; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: mmc:Mmcs_4396 thiamine pyrophosphate enzyme-like TPP-binding protein; Belongs to the TPP enzyme family.
 
 0.969
ilvC
Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
 
  
 0.967
Mvan_2128
KEGG: mpa:MAP3033c D-3-phosphoglycerate dehydrogenase; TIGRFAM: D-3-phosphoglycerate dehydrogenase; PFAM: amino acid-binding ACT domain protein; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic region; D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding.
  
  
 0.966
Mvan_5213
PFAM: thiamine pyrophosphate enzyme domain protein TPP-binding; thiamine pyrophosphate enzyme TPP binding domain protein; KEGG: mbo:Mb3539c probable acetohydroxyacid synthase IlvX (acetolactate synthase).
 
 0.964
ilvA
L-threonine ammonia-lyase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
 
 
 0.963
Your Current Organism:
Mycolicibacterium vanbaalenii
NCBI taxonomy Id: 350058
Other names: M. vanbaalenii PYR-1, Mycobacterium sp. PYR-1, Mycobacterium vanbaalenii DSM 7251, Mycobacterium vanbaalenii PYR-1, Mycolicibacterium vanbaalenii DSM 7251, Mycolicibacterium vanbaalenii PYR-1
Server load: medium (70%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.